SYNTHESIS AND PROPERTIES OF IMMOBILIZED ENZYMES .7. COUPLING OF GLYCOAMYLASE TO DIALDEHYDE CELLULOSE, CARBOXYMETHYLCELLOSE HYDRAZIDE AND CARBOXYMETHYLCELLULOSE AZIDE

  • 1 January 1977
    • journal article
    • research article
    • Vol. 36  (2) , 179-183
Abstract
Glucoamylase (.alpha.-1,4-glucan glucohydrolase, EC 3.2.1.3) was covalently linked to dialdehyde cellulose resulting in an immobilized enzyme containing 0.98% protein and an activity of 4.5 mg of the native enzyme/g of matrix, i.e., 46% relative activity. The complex lost its activity in continuous and batch hydrolysis of starch at 55.degree. C down to a limit of 18% of its original value. The activity of the complex did not change when working at a temperature of 25.degree. C. Glucoamylase-carboxymethylcellulose complexes synthesized via carboxymethylcellulose hydrazide and azide showed only an activity of 1 mg of the native enzyme/g of matrix. There was no success in coupling periodate-oxidized glucoamylase to carboxymethylcellulose hydrazide because the enzyme used lost nearly all of its activity during periodate oxidation.

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